Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.5.1.87 - ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q03175

for references in articles please use BRENDA:EC2.5.1.87
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme is involved in biosynthesis of dolichol (a long-chain polyprenol) with a saturated alpha-isoprene unit, which serves as a glycosyl carrier in protein glycosylation . The yeast Saccharomyces cerevisiae has two different enzymes that catalyse this reaction. Rer2p synthesizes a well-defined family of polyprenols of 13--18 isoprene residues with dominating C(80) (16 isoprene residues) extending to C(120), while Srt1p synthesizes mainly polyprenol with 22 isoprene subunits. Largest Srt1p products reach C(290) . The enzyme from Arabidopsis thaliana catalyses the formation of polyprenyl diphosphates with predominant carbon number C(120) .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: Q03175
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
dhdds, nogo-b receptor, rer2p, tk-idsb, srt1p, slcpt3, dedol-pp synthase, cis-ptase, dedolpp synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Srt2p Z-prenyltransferase
-
cis-prenyltransferase
-
Dedol-PP synthase
-
dehydrodolichyl diphosphate synthase
-
-
Rer2p Z-prenyltransferase
-
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 10–55 isopentenyl units)
The enzyme is involved in biosynthesis of dolichol (a long-chain polyprenol) with a saturated alpha-isoprene unit, which serves as a glycosyl carrier in protein glycosylation [1]. The yeast Saccharomyces cerevisiae has two different enzymes that catalyse this reaction. Rer2p synthesizes a well-defined family of polyprenols of 13--18 isoprene residues with dominating C(80) (16 isoprene residues) extending to C(120), while Srt1p synthesizes mainly polyprenol with 22 isoprene subunits. Largest Srt1p products reach C(290) [2]. The enzyme from Arabidopsis thaliana catalyses the formation of polyprenyl diphosphates with predominant carbon number C(120) [4].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate + 19 isopentenyl diphosphate
19 diphosphate + di-trans,poly-cis-docosaprenyl diphosphate
show the reaction diagram
-
dominating polyprenol with 22 isoprene residues, Srt1p products reaching C290 indicate the failure of a strict bacterial-like chain length control
-
?
(2E,6E)-farnesyl diphosphate + 13 isopentenyl diphosphate
13 diphosphate + di-trans,poly-cis-hexadecaprenyl diphosphate
show the reaction diagram
(2E,6E)-farnesyl diphosphate + 14 isopentenyl diphosphate
14 diphosphate + di-trans,poly-cis-heptadecaprenyl diphosphate
show the reaction diagram
-
di-trans,poly-cis-hexadecaprenyl diphosphate and di-trans,poly-cis-heptadecaprenyl diphosphate are the main products
-
?
(2E,6E)-farnesyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + di-trans,poly-cis-octaprenyl diphosphate
show the reaction diagram
(2E,6E)-farnesyl diphosphate + 6 isopentenyl diphosphate
6 diphosphate + di-trans,poly-cis-nonaprenyl diphosphate
show the reaction diagram
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + di-trans,poly-cis-polyprenyl diphosphate
show the reaction diagram
-
-
-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate (n: 10-55)
show the reaction diagram
-
-
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2E,6E)-farnesyl diphosphate + 19 isopentenyl diphosphate
19 diphosphate + di-trans,poly-cis-docosaprenyl diphosphate
show the reaction diagram
-
dominating polyprenol with 22 isoprene residues, Srt1p products reaching C290 indicate the failure of a strict bacterial-like chain length control
-
?
(2E,6E)-farnesyl diphosphate + 13 isopentenyl diphosphate
13 diphosphate + di-trans,poly-cis-hexadecaprenyl diphosphate
show the reaction diagram
(2E,6E)-farnesyl diphosphate + 14 isopentenyl diphosphate
14 diphosphate + di-trans,poly-cis-heptadecaprenyl diphosphate
show the reaction diagram
-
di-trans,poly-cis-hexadecaprenyl diphosphate and di-trans,poly-cis-heptadecaprenyl diphosphate are the main products
-
?
(2E,6E)-farnesyl diphosphate + 5 isopentenyl diphosphate
5 diphosphate + di-trans,poly-cis-octaprenyl diphosphate
show the reaction diagram
the polyprenol product of Srt1p is longer in chain length than that of Rer2p and is not sufficiently converted to dolichol and dolichyl phosphate, unlike that of Rer2p
di-trans,poly-cis-octaprenyl diphosphate and di-trans,poly-cis-nonaprenyl diphosphate are the main products
-
?
(2E,6E)-farnesyl diphosphate + 6 isopentenyl diphosphate
6 diphosphate + di-trans,poly-cis-nonaprenyl diphosphate
show the reaction diagram
the polyprenol product of Srt1p is longer in chain length than that of Rer2p and is not sufficiently converted to dolichol and dolichyl phosphate, unlike that of Rer2p
di-trans,poly-cis-octaprenyl diphosphate and di-trans,poly-cis-nonaprenyl diphosphate are the main products
-
?
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate
n diphosphate + ditrans,polycis-polyprenyl diphosphate (n: 10-55)
show the reaction diagram
-
-
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
5 mM used in assay conditions
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Srt1p resides mostly in lipid particles
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
rer2 mutant is defective in both N- and O-linked glycosylation in the endoplasmic reticulum, the rer2 mutant is deficient in the activity of cis-prenyltransferase, a key enzyme of dolichol synthesis
physiological function
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
on the basis of Escherichia coli undecaprenyl diphosphate synthase crystallographic structure the yeast Rer2p model is constructed. In the model three amino acid residues inserted into the sequence corresponding to the floor region of the tunnel extends the bottom loop what results in the required increase of the tunnel volume. Thermal fluctuations of this loop occasionally create a hole in the tunnel floor, making escape of polyprenol omega end out of the tunnel possible what switches off the control mechanism of product length thereby allowing a practically unlimited elongation process leading to an exponential distribution of longer chain polyprenols
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
over-expression of SRT1 suppresses the growth and glycosylation defects of rer2
when GFP-RER2 is over-expressed under the TDH3 promoter in DELTArer2, a continuous endioplasmic reticulum pattern and some dots associated with the endoplasmic reticulum are observed in the early logarithmic phase
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Srt1p is expressed in stationary phase with dominating polyprenol with 22 isoprene residues
induced in the stationary phase
mainly expressed in the early logarithmic phase
Rer2p is active in logarithmic phase, with dominating polyprenol with 16 isoprene residues
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Poznanski, J.; Szkopinska, A.
Precise bacterial polyprenol length control fails in Saccharomyces cerevisiae
Biopolymers
86
155-164
2007
Saccharomyces cerevisiae (P35196), Saccharomyces cerevisiae (Q03175), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Sato, M.; Fujisaki, S.; Sato, K.; Nishimura, Y.; Nakano, A.
Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis
Genes Cells
6
495-506
2001
Saccharomyces cerevisiae (C7GM47), Saccharomyces cerevisiae (P35196), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Sato, M.; Sato, K.; Nishikawa, S.; Hirata, A.; Kato, J.; Nakano, A.
The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis
Mol. Cell. Biol.
19
471-483
1999
Saccharomyces cerevisiae (C7GM47), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Park, E.J.; Grabinska, K.A.; Guan, Z.; Stranecky, V.; Hartmannova, H.; Hodanova, K.; Baresova, V.; Sovova, J.; Jozsef, L.; Ondruskova, N.; Hansikova, H.; Honzik, T.; Zeman, J.; Hulkova, H.; Wen, R.; Kmoch, S.; Sessa, W.C.
Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation
Cell Metab.
20
448-457
2014
Saccharomyces cerevisiae (Q12063), Saccharomyces cerevisiae, Homo sapiens (Q96E22), Homo sapiens, Mus musculus (Q99LJ8), Schizosaccharomyces pombe (Q9Y7K8), Saccharomyces cerevisiae BY4742 (Q12063)
Manually annotated by BRENDA team
Kwon, M.; Kwon, E.J.; Ro, D.K.
cis-Prenyltransferase and polymer analysis from a natural rubber perspective
Methods Enzymol.
576
121-145
2016
Saccharomyces cerevisiae, Arabidopsis thaliana (O80458)
Manually annotated by BRENDA team